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Yorodumi- PDB-1rot: STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BI... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1rot | ||||||
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Title | STRUCTURE OF FKBP59-I, THE N-TERMINAL DOMAIN OF A 59 KDA FK506-BINDING PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE | ||||||
Components | FKBP59-I | ||||||
Keywords | ROTAMASE (ISOMERASE) / DOMAIN I (N-TERM) OF A 59 KDA / FK506-BINDING PROTEIN / PEPTIDYL PROLYL CIS-TRANS ISOMERASE | ||||||
Function / homology | Function and homology information negative regulation of microtubule polymerization or depolymerization / axonal growth cone / chaperone-mediated protein folding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / tau protein binding / negative regulation of neuron projection development / microtubule / mitochondrion / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Oryctolagus cuniculus (rabbit) | ||||||
Method | SOLUTION NMR | ||||||
Authors | Craescu, C.T. / Rouviere, N. / Popescu, A. / Cerpolini, E. / Lebeau, M.-C. / Baulieu, E.-E. / Mispelter, J. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: Three-dimensional structure of the immunophilin-like domain of FKBP59 in solution. Authors: Craescu, C.T. / Rouviere, N. / Popescu, A. / Cerpolini, E. / Lebeau, M.C. / Baulieu, E.E. / Mispelter, J. #1: Journal: Eur.J.Biochem. / Year: 1995 Title: 1H and 15N Assignment of NMR Spectrum, Secondary Structure and Global Folding of the Immunophilin-Like Domain of the 59-kDa Fk506-Binding Protein Authors: Rouviere-Fourmy, N. / Craescu, C.T. / Mispelter, J. / Lebeau, M.C. / Baulieu, E.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1rot.cif.gz | 48.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1rot.ent.gz | 34.1 KB | Display | PDB format |
PDBx/mmJSON format | 1rot.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ro/1rot ftp://data.pdbj.org/pub/pdb/validation_reports/ro/1rot | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 16259.305 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Oryctolagus cuniculus (rabbit) / Organ: LIVER / Production host: Escherichia coli (E. coli) / References: UniProt: P27124 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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-Sample preparation
Sample conditions | pH: 6.7 / Temperature units: K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-Processing
NMR software | Name: Discover / Developer: BIOSYM / Classification: refinement |
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Refinement | Software ordinal: 1 / Details: CVFF OF DISCOVER (BIOSYM) |
NMR ensemble | Conformer selection criteria: MINIMIZED AVERAGE / Conformers submitted total number: 1 |